PDB-4k2h: Crystal structure of C103A mutant of DJ-1 superfamily protein STM...

ID or keywords:

Entry

Database: PDB / ID: 4k2h

Title

Crystal structure of C103A mutant of DJ-1 superfamily protein STM1931 from Salmonella typhimurium

Components

Intracellular protease/amidase

Keywords

UNKNOWN FUNCTION / Structural Genomics / Center for Structural Genomics of Infectious Diseases / CSGID

Function / homology

Function and homology information

protein deglycation, glyoxal removal / guanine deglycation, glyoxal removal / protein deglycase activity / peptidase activity / metal ion binding / cytosol
Similarity search - Function

Biological species

Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.2 Å

Authors

Shumilin, I.A. / Niedzialkowska, E. / Domagalski, M.J. / Stam, J. / Anderson, W.F. / Minor, W. / Center for Structural Genomics of Infectious Diseases (CSGID)

Citation

Journal: TO BE PUBLISHED
Title: Crystal structure of C103A mutant of DJ-1 superfamily protein STM1931 from Salmonella typhimurium
Authors: Shumilin, I.A. / Niedzialkowska, E. / Domagalski, M.J. / Stam, J. / Anderson, W.F. / Minor, W. / Center for Structural Genomics of Infectious Diseases (CSGID)

History

Deposition	Apr 9, 2013	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 24, 2013	Provider: repository / Type: Initial release
Revision 1.1	Nov 15, 2017	Group: Refinement description / Category: software
Revision 1.2	Apr 13, 2022	Group: Database references / Derived calculations / Structure summary Category: audit_author / citation_author ...audit_author / citation_author / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _audit_author.identifier_ORCID / _citation_author.identifier_ORCID ..._audit_author.identifier_ORCID / _citation_author.identifier_ORCID / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3	Sep 20, 2023	Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	4k2h.cif.gz	975.7 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	4k2h_validation.pdf.gz	533.8 KB	Display	wwPDB validaton report
Full document	4k2h_full_validation.pdf.gz	552 KB	Display
Data in XML	4k2h_validation.xml.gz	98 KB	Display
Data in CIF	4k2h_validation.cif.gz	138.2 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/k2/4k2h ftp://data.pdbj.org/pub/pdb/validation_reports/k2/4k2h	HTTPS FTP

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Related structure data

Related structure data	4e08S S: Starting model for refinement
Similar structure data	1l9e-1 5zbk-1 1l9e-2 1el5-2 1el7-1 2fex-1 3bhf-2 3qss-2 3qsm-1 1l9d-1 Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - FunctionF&H Search Similarity search - HomologyF&H Search
Other databases	TargetTrack: IDP01948

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#215 - Nov 2017 Aspartate Transcarbamoylase similarity (1) #57 - Sep 2004 Catalase similarity (1)

Deposited unit

A: Intracellular protease/amidase

B: Intracellular protease/amidase

C: Intracellular protease/amidase

D: Intracellular protease/amidase

E: Intracellular protease/amidase

F: Intracellular protease/amidase

G: Intracellular protease/amidase

H: Intracellular protease/amidase

I: Intracellular protease/amidase

J: Intracellular protease/amidase

K: Intracellular protease/amidase

L: Intracellular protease/amidase

M: Intracellular protease/amidase

N: Intracellular protease/amidase

hetero molecules

280 kDa, 14 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Intracellular protease/amidase

B: Intracellular protease/amidase

hetero molecules

defined by author&software
40 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Intracellular protease/amidase

D: Intracellular protease/amidase

hetero molecules

defined by author&software
40 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

E: Intracellular protease/amidase

F: Intracellular protease/amidase

hetero molecules

defined by author&software
40 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

G: Intracellular protease/amidase

H: Intracellular protease/amidase

hetero molecules

defined by author&software
40 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

5

I: Intracellular protease/amidase

J: Intracellular protease/amidase

hetero molecules

defined by author&software
40 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

6

K: Intracellular protease/amidase

L: Intracellular protease/amidase

hetero molecules

defined by author&software
40 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

7

M: Intracellular protease/amidase

N: Intracellular protease/amidase

hetero molecules

defined by author&software
40 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	179.662, 113.751, 175.710
Angle α, β, γ (deg.)	90.000, 109.330, 90.000
Int Tables number	5
Space group name H-M	C121

#1: Protein	Intracellular protease/amidase Mass: 19942.830 Da / Num. of mol.: 14 / Mutation: C103A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium (bacteria) Strain: LT2 / Gene: araH, STM1931 / Plasmid: pMCSG7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21-CodonPlus(DE3)-RIPL / References: UniProt: Q8ZNU7
#2: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: Zn
#3: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1183 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 3.03 Å³/Da / Density % sol: 59.46 %
Crystal grow	Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.1M bis-tris propane, 0.9M DL-malic acid, 0.005M zinc chloride, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 19-ID / Wavelength: 0.97857 Å

Detector

Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 11, 2012 / Details: MIRROR

Radiation

Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 0.97857 Å / Relative weight: 1

Reflection

Resolution: 2.2→50 Å / Num. obs: 169402 / % possible obs: 94.9 % / Observed criterion σ(I): -3 / Redundancy: 2.1 % / B_iso Wilson estimate: 39.7 Å² / R_merge(I) obs: 0.069 / Χ²: 2.111 / Net I/σ(I): 9.6

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique all	Χ²	Diffraction-ID	% possible all
2.2-2.24	2	0.41	8494	1.207	1	96.1
2.24-2.28	2	0.371	8523	1.231	1	96
2.28-2.32	2	0.336	8562	1.304	1	96.1
2.32-2.37	2	0.328	8518	1.301	1	95.9
2.37-2.42	2	0.282	8519	1.32	1	95.7
2.42-2.48	2	0.246	8579	1.434	1	96.1
2.48-2.54	2	0.225	8497	1.541	1	95.7
2.54-2.61	2	0.184	8483	1.652	1	95.7
2.61-2.69	2	0.167	8513	1.79	1	95.2
2.69-2.77	2.1	0.146	8481	1.852	1	95.2
2.77-2.87	2.1	0.129	8459	1.967	1	95
2.87-2.99	2.1	0.116	8430	2.147	1	95
2.99-3.12	2.1	0.096	8450	2.45	1	94.2
3.12-3.29	2	0.082	8365	2.628	1	93.7
3.29-3.49	2	0.075	8315	2.976	1	93.1
3.49-3.76	2	0.065	8300	3.209	1	93.2
3.76-4.14	2	0.056	8336	3.197	1	93.1
4.14-4.74	2	0.049	8429	3.241	1	94.1
4.74-5.97	2.1	0.044	8640	2.828	1	95.9
5.97-50	2.4	0.041	8509	2.784	1	93.1

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
MOLREP		phasing
REFMAC		refinement
PDB_EXTRACT	3.11	data extraction
HKL-3000		data collection
HKL-3000		data reduction
HKL-3000		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4E08

4e08

Resolution: 2.2→36.71 Å / Cor.coef. F_o:F_c: 0.968 / Cor.coef. F_o:F_c free: 0.956 / WR_factor R_free: 0.1966 / WR_factor R_work: 0.166 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.8492 / SU B: 9.886 / SU ML: 0.128 / SU R Cruickshank DPI: 0.2141 / SU R_free: 0.1722 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.214 / ESU R Free: 0.172 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2046	8016	5 %	RANDOM
R_work	0.1715	-	-	-
obs	0.1731	160372	94.79 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso max: 116.41 Å² / B_iso mean: 42.6984 Å² / B_iso min: 11.98 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.25 Å²	-0 Å²	-2.01 Å²
2-	-	-1.05 Å²	-0 Å²
3-	-	-	1.22 Å²

Refinement step

Cycle: LAST / Resolution: 2.2→36.71 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19400	0	14	1183	20597

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.01	0.019	20028
X-RAY DIFFRACTION	r_bond_other_d	0	0.02	19547
X-RAY DIFFRACTION	r_angle_refined_deg	1.335	1.97	27346
X-RAY DIFFRACTION	r_angle_other_deg	3.62	3	44832
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	5.649	5	2636
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	35.093	23.341	823
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	13.913	15	3092
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.29	15	148
X-RAY DIFFRACTION	r_chiral_restr	0.076	0.2	3171
X-RAY DIFFRACTION	r_gen_planes_refined	0.006	0.021	22941
X-RAY DIFFRACTION	r_gen_planes_other	0.007	0.02	4399

LS refinement shell

Resolution: 2.2→2.257 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.276	583	-
R_work	0.242	11399	-
all	-	11982	-
obs	-	-	96.06 %

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	1.1379	-0.7675	0.3083	0.5662	-0.0198	0.9903	0.034	-0.0054	-0.0328	-0.0325	0.0265	0.0142	0.0483	0.0707	-0.0605	0.0963	0.0093	0.0693	0.1835	0.0144	0.1045	84.316	0.326	-18.956
2	1.4048	0.0157	0.8594	1.1695	0.2531	0.5884	0.0231	0.1822	0.1604	-0.1268	-0.0901	-0.1698	-0.0089	0.1407	0.067	0.098	0.0212	0.0944	0.2268	0.0492	0.1075	93.634	8.605	-26.457
3	1.4182	0.1121	0.1595	1.2512	0.3088	0.2238	0.0201	-0.0473	0.0361	0.012	0.0081	0.0997	0.029	0.0388	-0.0282	0.1085	-0.0164	0.0689	0.1704	0.029	0.1154	67.483	11.976	-16.535
4	0.6549	0.0289	0.1924	0.1707	-0.1699	0.4513	-0.0385	0.0838	0.1012	-0.0134	-0.0056	0.0624	-0.0055	0.0431	0.0441	0.1084	-0.0138	0.0698	0.1645	0.0346	0.1326	65.156	20.904	-27.044
5	1.8493	-0.8409	0.7016	3.3391	-2.3976	1.7392	0.0031	-0.0862	0.0524	-0.0486	-0.0893	-0.1146	0.0344	0.0115	0.0862	0.1109	-0.0212	0.0736	0.1863	-0.0516	0.1066	30.631	14.102	-28.12
6	0.7943	-0.0523	0.2721	0.2511	0.0898	0.2377	0.0129	-0.0699	0.0577	-0.001	-0.0076	-0.0421	0.0214	-0.0599	-0.0053	0.1033	0.0032	0.0759	0.1627	-0.0351	0.1238	32.26	18.285	-23.222
7	1.0891	0.7279	0.443	0.5611	0.138	0.8248	0.0729	-0.1092	0.025	0.0105	-0.0305	0.0074	0.0915	-0.068	-0.0424	0.0991	-0.0437	0.0724	0.1847	0.0091	0.1036	11.057	0.693	-27.84
8	1.8574	-0.054	1.4478	0.867	-0.157	1.1505	0.0624	-0.2779	0.1992	0.1801	-0.1746	0.1786	0.0044	-0.1939	0.1122	0.1027	-0.0493	0.1007	0.2342	-0.0567	0.1107	5.572	10.708	-17.875
9	0.9894	-0.0027	0.5984	0.2888	0.0324	1.052	0.0421	0.0183	-0.0402	0.0271	-0.0282	0.0281	-0.0974	0.0618	-0.0139	0.1032	-0.0383	0.0743	0.1552	0.0403	0.1127	-13.136	-7.42	-43.34
10	1.3212	-0.1324	0.4933	0.6308	0.0894	0.4843	0.1632	-0.001	-0.1069	0.0917	-0.0602	0.0219	0.1286	-0.0195	-0.103	0.1079	-0.0152	0.0559	0.1592	0.0628	0.1516	-16.978	-20.648	-37.736
11	1.0703	-0.0823	0.755	0.0732	0.0888	1.4157	0.0559	0.0105	-0.0889	-0.0343	-0.0232	0.0691	0.0248	0.0488	-0.0326	0.1035	0.0363	0.0177	0.15	-0.0271	0.1292	-24.2	-14.387	-66.906
12	1.6549	-0.0846	0.3476	0.0587	-0.2985	1.586	0.1642	-0.1089	-0.3592	-0.0688	0.0041	0.049	0.3923	-0.066	-0.1683	0.1522	-0.0149	-0.0043	0.0816	-0.0098	0.1745	-27.128	-27.872	-60.888
13	1.5019	-0.621	0.4052	1.0615	-0.1838	0.3376	0.0509	0.0399	0.0091	0.032	0.0673	-0.0226	0.0841	0.0369	-0.1182	0.069	0.0382	0.0069	0.1556	-0.0398	0.1322	-45.357	-9.288	-87.189
14	3.545	-0.0288	1.5481	1.5337	-0.3692	0.9008	0.3225	0.5081	-0.1107	-0.3971	-0.1913	-0.2549	0.2142	0.3326	-0.1312	0.1376	0.1055	0.0679	0.244	-0.0909	0.1971	-38.637	-11.77	-100.287
15	1.563	0.6631	0.8991	1.3415	0.5824	0.7075	0.0002	-0.0746	0.1212	0.0487	0.0383	0.0263	0.0312	-0.0344	-0.0385	0.0324	0.0033	0.0341	0.144	-0.0413	0.1818	-59.673	8.195	-67.127
16	2.4423	0.2925	1.0049	1.4741	-0.3977	0.6404	0.3109	-0.593	0.2959	0.5145	-0.3035	0.285	-0.0145	-0.169	-0.0074	0.2406	-0.1071	0.1103	0.2841	-0.0863	0.1165	-66.49	5.815	-54.128
17	1.6714	-0.5147	0.1028	0.2657	-0.1245	0.5077	-0.0171	-0.0101	-0.0474	-0.002	-0.0879	0.0577	-0.0623	0.0044	0.105	0.0644	0.0069	0.044	0.1433	-0.0441	0.1807	-31.201	14.114	-59.517
18	1.6444	-0.0225	0.2124	0.1543	-0.288	0.8921	0.001	-0.0031	0.3308	0.0243	-0.0847	0.0225	-0.2308	0.0229	0.0837	0.1301	0.0574	0.0038	0.0987	-0.0567	0.2006	-30.054	28.902	-61.058
19	1.2544	-0.0395	0.0893	0.3158	0.0621	0.4914	-0.0138	0.0535	-0.0136	-0.022	-0.064	0.0237	-0.0234	0.0978	0.0778	0.0794	-0.0173	0.0684	0.1812	0.0572	0.1096	-5.227	11.483	-65.46
20	1.4477	-0.089	0.55	0.1527	0.2101	0.8677	0.0057	0.1664	0.424	-0.0226	-0.064	-0.078	-0.1558	0.0261	0.0583	0.1328	-0.0722	0.025	0.1451	0.1024	0.1818	-4.228	26.273	-67.162
21	2.0443	-0.5146	1.2937	1.5202	-0.9947	1.1841	0.0847	0.2536	-0.0101	-0.0464	-0.0049	0.0759	0.082	0.1131	-0.0798	0.0699	0.0272	0.0415	0.2174	0.0141	0.0884	22.032	3.883	-56.137
22	4.5609	-0.4519	2.4093	2.493	0.5213	1.5088	0.7133	1.2813	-0.1071	-0.6921	-0.5701	-0.2368	0.1913	0.5408	-0.1432	0.2986	0.2695	0.0726	0.508	-0.0309	0.055	29.683	-0.745	-68.24
23	1.9601	-0.5802	0.8685	1.2782	-0.5601	0.4838	0.1896	0.0623	-0.2215	-0.0247	-0.0399	0.0721	0.0706	0.0519	-0.1497	0.1291	0.0514	0.0007	0.1368	-0.0727	0.1611	37.321	-12.676	-41.306
24	4.6514	0.0736	1.761	1.6585	-0.067	0.6976	0.3747	0.4338	-0.2264	-0.4074	-0.2503	-0.2431	0.2151	0.2299	-0.1244	0.2301	0.1707	-0.02	0.2518	-0.157	0.2186	44.079	-17.373	-53.856
25	0.9299	-0.3293	0.0881	0.4818	0.134	1.1505	0.0584	0.0018	-0.0686	-0.0833	0.0236	0.1391	0.0161	0.1235	-0.082	0.1129	-0.0303	0.0188	0.1515	0.0294	0.1244	62.92	-14.022	-17.85
26	0.8418	0.159	0.2739	0.1399	0.2482	1.3349	0.0708	-0.0461	-0.1508	-0.0087	-0.018	0.0783	0.2548	-0.0407	-0.0528	0.1567	-0.0182	-0.0411	0.1138	0.0046	0.2168	54.061	-24.846	-17.726
27	3.6415	-0.2803	-2.3722	0.3903	1.1269	3.9974	0.0392	0.0192	0.0957	-0.0002	0.0512	0.0048	-0.0262	0.0657	-0.0904	0.1144	-0.0334	0.059	0.1541	0.0866	0.1226	65.566	-9.192	1.402
28	0.5354	0.1112	0.3179	0.2847	0.1226	0.6068	0.029	-0.04	-0.0416	0.0216	0.0202	0.0409	0.0142	0.053	-0.0492	0.0919	-0.0372	0.0726	0.1839	0.0579	0.1192	67.326	-13.45	6.143

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	1 - 88
2	X-RAY DIFFRACTION	2	A	89 - 185
3	X-RAY DIFFRACTION	3	B	1 - 61
4	X-RAY DIFFRACTION	4	B	62 - 185
5	X-RAY DIFFRACTION	5	C	1 - 18
6	X-RAY DIFFRACTION	6	C	19 - 185
7	X-RAY DIFFRACTION	7	D	0 - 115
8	X-RAY DIFFRACTION	8	D	116 - 185
9	X-RAY DIFFRACTION	9	E	1 - 114
10	X-RAY DIFFRACTION	10	E	115 - 185
11	X-RAY DIFFRACTION	11	F	1 - 116
12	X-RAY DIFFRACTION	12	F	117 - 185
13	X-RAY DIFFRACTION	13	G	0 - 114
14	X-RAY DIFFRACTION	14	G	115 - 185
15	X-RAY DIFFRACTION	15	H	1 - 114
16	X-RAY DIFFRACTION	16	H	115 - 185
17	X-RAY DIFFRACTION	17	I	1 - 114
18	X-RAY DIFFRACTION	18	I	115 - 185
19	X-RAY DIFFRACTION	19	J	1 - 114
20	X-RAY DIFFRACTION	20	J	115 - 185
21	X-RAY DIFFRACTION	21	K	1 - 116
22	X-RAY DIFFRACTION	22	K	117 - 185
23	X-RAY DIFFRACTION	23	L	1 - 114
24	X-RAY DIFFRACTION	24	L	115 - 185
25	X-RAY DIFFRACTION	25	M	1 - 62
26	X-RAY DIFFRACTION	26	M	63 - 185
27	X-RAY DIFFRACTION	27	N	1 - 18
28	X-RAY DIFFRACTION	28	N	19 - 185

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